TRI50_PIG
ID TRI50_PIG Reviewed; 486 AA.
AC Q865W2;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM50;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q86XT4};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM50 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 50;
GN Name=TRIM50;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ucla C., Merla G., Meroni G., Reymond A.;
RT "Novel genes in the Williams-Beuren Syndrome critical region.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that ubiquitinates Beclin-1/BECN1
CC in a 'Lys-63'-dependent manner enhancing its binding to ULK1. In turn,
CC promotes starvation-induced autophagy activation. Interacts also with
CC p62/SQSTM1 protein and thereby induces the formation and the autophagy
CC clearance of aggresome-associated polyubiquitinated proteins through
CC HDAC6 interaction. {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q86XT4};
CC -!- SUBUNIT: Can form dimers and trimers. Interacts with several E2
CC ubiquitin-conjugating enzymes, including UBE2L6, UBE2E1, UBE2E3. No
CC interaction with UBE2H. Interacts with BECN1. Interacts with SQSTM1.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XT4}.
CC Note=Localizes mainly into discrete cytoplasmic punctuate structures
CC heterogeneous in size and shape containing polyubiquitinated proteins.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- PTM: Acetylated by EP300 and KAT2B. HDAC6 drives TRIM50 deacetylation.
CC Acetylation antagonizes with TRIM50 ubiquitination.
CC {ECO:0000250|UniProtKB:Q86XT4}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY081951; AAL91074.1; -; mRNA.
DR RefSeq; NP_999351.1; NM_214186.1.
DR AlphaFoldDB; Q865W2; -.
DR SMR; Q865W2; -.
DR STRING; 9823.ENSSSCP00000008227; -.
DR PaxDb; Q865W2; -.
DR GeneID; 397383; -.
DR KEGG; ssc:397383; -.
DR CTD; 135892; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q865W2; -.
DR OrthoDB; 574602at2759; -.
DR TreeFam; TF342569; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q865W2; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..486
FT /note="E3 ubiquitin-protein ligase TRIM50"
FT /id="PRO_0000056276"
FT DOMAIN 275..474
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 84..125
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 125..170
FT /evidence="ECO:0000255"
FT COILED 204..235
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q810I2"
SQ SEQUENCE 486 AA; 54776 MW; A33A8D06EFC7A7F1 CRC64;
MAWQVSVPEL EDRLQCPVCL EVFKEPLMLQ CGHSYCKGCL LSLSRHLDSE LRCPVCRQEV
DSSSSPPNVS LARVIEALQL PGDPEPQVCT HHRNPLSLFC EKDQELICGL CGLLGSHQHH
RVTPVSTVYS RMKEELAALI SDLKQEQKKV EEQVAKLVNN RTRIVNESDV FSWVIRREFQ
ELHHLVDEEK ARCLEGVEGH TRGLVASLDM QLEQARGAQE RLAQATCMLE QFGNESHYEF
IRYHSTASSA ELQQARLLEG AFSPISFKPG LHQADIKLTV WKRLFRKVLP APESLKLDPT
TAHPLLELSK GNTVVQCGLL AQRRASQPER FDYSTCVLAS RGFSCGRHYW EVVVGSKSDW
RLGVIKGTAS RKGKLNKSPE HGVWLIGLKE GRVYEAFSCP RVPLPVAGHP HRIGVYLHYE
QGELTFFDAD RPDDLRLLYT FQADFQGKLY PILDTCWHER GSNSLPMVLP LPSGPGHLTP
SQPTKL
